LOCUS       NP_786939               1320 aa            linear   ROD 27-APR-2025
DEFINITION  immunoglobulin superfamily member 1 precursor [Rattus norvegicus].
ACCESSION   NP_786939
VERSION     NP_786939.1
DBSOURCE    REFSEQ: accession NM_175763.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1320)
  AUTHORS   Wang,Y., Brule,E., Silander,T., Bak,B., Joustra,S.D. and
            Bernard,D.J.
  TITLE     The short mRNA isoform of the immunoglobulin superfamily, member 1
            gene encodes an intracellular glycoprotein
  JOURNAL   PLoS One 12 (7), e0180731 (2017)
   PUBMED   28686733
  REMARK    GeneRIF: Contrary to earlier predictions, neither the murine nor
            rat IGSF1-2 is secreted from heterologous or homologous cells. In
            addition, neither protein associates with the plasma membrane.
            Rather, IGSF1-2 appears to be retained in the endoplasmic
            reticulum.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1320)
  AUTHORS   Joustra,S.D., Meijer,O.C., Heinen,C.A., Mol,I.M., Laghmani el,H.,
            Sengers,R.M., Carreno,G., van Trotsenburg,A.S., Biermasz,N.R.,
            Bernard,D.J., Wit,J.M., Oostdijk,W., van Pelt,A.M., Hamer,G. and
            Wagenaar,G.T.
  TITLE     Spatial and temporal expression of immunoglobulin superfamily
            member 1 in the rat
  JOURNAL   J Endocrinol 226 (3), 181-191 (2015)
   PUBMED   26163525
  REMARK    GeneRIF: High levels of Igsf1 in brain, pituitary and fetal liver.
            Also expressed in pancreas, heart, skeletal muscle, adrenal gland
            and testis.
REFERENCE   3  (residues 1 to 1320)
  AUTHORS   Chapman,S.C. and Woodruff,T.K.
  TITLE     Modulation of activin signal transduction by inhibin B and
            inhibin-binding protein (INhBP)
  JOURNAL   Mol Endocrinol 15 (4), 668-679 (2001)
   PUBMED   11266516
REFERENCE   4  (residues 1 to 1320)
  AUTHORS   Bernard,D.J. and Woodruff,T.K.
  TITLE     Inhibin binding protein in rats: alternative transcripts and
            regulation in the pituitary across the estrous cycle
  JOURNAL   Mol Endocrinol 15 (4), 654-667 (2001)
   PUBMED   11266515
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF322216.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF322216.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5756307,
                                           SAMEA5760383 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1320
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq36"
     Protein         1..1320
                     /product="immunoglobulin superfamily member 1 precursor"
                     /note="inhibin-binding protein"
                     /calculated_mol_wt=145117
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
                     /calculated_mol_wt=2195
     mat_peptide     19..1320
                     /product="Immunoglobulin superfamily member 1.
                     /id=PRO_0000318514"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N6.1)"
                     /calculated_mol_wt=145117
     Region          28..114
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            44
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          45..49
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          57..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          80..84
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          94..99
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          109..112
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          122..212
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          139..143
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          151..155
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          173..177
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          187..192
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          205..208
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          218..307
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          235..239
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          247..251
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          270..274
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          284..289
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          300..303
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          320..405
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            329
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          330..334
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          342..346
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            365
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          366..370
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          380..385
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          395..401
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          407..488
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          419..423
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          431..435
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          449..453
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          463..468
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          481..484
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            505..525
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N6.1)"
     Site            535..555
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          575..663
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            591
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          592..596
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          605..609
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          627..631
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          641..646
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          656..659
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          669..756
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          683..687
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          695..699
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          717..721
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          731..736
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            731
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          749..752
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          762..852
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          779..783
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            782
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          791..795
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          816..820
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          830..835
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            830
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          845..848
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          858..944
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            874
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          875..879
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          887..891
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          909..913
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          923..928
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            923
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          941..944
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          954..1044
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            970
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          971..975
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          983..987
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1005..1009
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            1011
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          1019..1024
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1037..1040
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1050..1140
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            1066
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          1067..1071
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Region          1079..1083
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Region          1101..1105
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Region          1115..1120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Site            1131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          1133..1136
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     Region          1146..1232
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1163..1167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1175..1179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1193..1197
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1207..1212
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            1207
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q925N6.1)"
     Region          1225..1228
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..1320
                     /gene="Igsf1"
                     /gene_synonym="Inhbp"
                     /coded_by="NM_175763.2:172..4134"
                     /db_xref="GeneID:302822"
                     /db_xref="RGD:631402"
ORIGIN      
        1 mmlrtftlll lciwlnrgmt smaavesqpe lwiesnypqa pwenitlwck spsrvsskfl
       61 llkdntqmtw ihppyktfqv sffigaltes ntglyrccyw nekgwskpsk ileleapgql
      121 pkpifwiqae tppfpgcnvn ilchgwlqdl vfmlfkegyt epidyqvptg tmaifsidnl
      181 apenegiyic rthiqmlptl wsepsnplkl vvaglypkpt ltahpgpila pgeslslrcq
      241 gpiygmtfal mrledlkkpy yykkpiknea yfyfqalktq dtghylcfyy dgsyrgslls
      301 dilkiwvtdt fpktwllvqp spviqmgqnv slrcgglmdg vglalhkkge ekplqfldat
      361 sntgnnsffl knvtyrdagi yschyyltwk tsikmatynt velivvawps svfkvgktit
      421 lqcrvshpvl efsleweett tfqkfsvdgd fiitniegqg tgtyscsyri eshaniwshr
      481 seplklvgpa vtgflpwnsi lneairvslt vqflsllllv lwlqwkcrrl rlreawllgt
      541 aqgvamlvil iallccglcn galteeieii mptpkpelwa etnfpqapwk nvtlwcrsps
      601 gstkefvllk dgtgwiatrp aseqvraafp lgaltqshtg syhchsweem avsepseale
      661 lvgtdilpkp visaslpirg qelqirckgw leglgfalyk mgeqepvqql gavgreafft
      721 iqrmedkeeg nyscrthtek qpfkwsepsa plelvikely pkpffktwas pvvtpgsrvt
      781 fncstsrehm sfilykdgne iassdpvwgn pgtstahfli isvgigdggn yscryydfsi
      841 wsepsdpvel ivtefypkpt llaqpgpvvl pgknvtlrcq gifqgmrfal lqegahaplq
      901 fqsasgtsvd fllhtvgaed fgnyscvyye ttmsnrgsyl stplmiwvtd tfprpwlsae
      961 pssvvtmgqn vtlwcqgpvh gvgyilhkeg eatsmqlwds tsnegafpii nisgasigry
     1021 sccyhpdwms pikiqpsntl elivtgllpk psllvqpgpm vvpgenmtfq cqgelpdstf
     1081 vllkegtqqp ieqqrpsgyr adfwmpvvrd qdsgvyscvy yldsaplvas nhsnsleiwv
     1141 tdkppkpsls awpstvfklg kditlqcrgp lpgvefvleh dgeeapqqfs edgdfvignm
     1201 egkgignysc syrlqaypdi wsepsdslel vgaagpvaqe ctvgnivrst livvvvvalg
     1261 ivlaiewkkw prlrtrgset dgrdqtivle ecnqdgepgt atnspssalq gvsveqtvpi
//
