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Q8N6C5 (IGSF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Immunoglobulin superfamily member 1

Short name=IgSF1
Alternative name(s):
Immunoglobulin-like domain-containing protein 1
Inhibin-binding protein
Short name=InhBP
Pituitary gland-specific factor 2
p120
Gene names
Name:IGSF1
Synonyms:IGDC1, KIAA0364, PGSF2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to be a coreceptor in inhibin signaling, but seems not to be a high-affinity inhibin receptor. Antagonizes activin A signaling in the presence or absence of inhibin B By similarity. Necessary to mediate a specific antagonistic effect of inhibin B on activin-stimulated transcription. Ref.7

Subunit structure

Interacts with INHA By similarity. In Ref.9 does not interact with INHA; standard receptor binding assay. Interacts with ACVR1B; the interaction appears to be ligand-dependent as it is diminished by inhibin B and activin A. Interacts with ACVR2A, ACVR2B, ACVRL1 and BMPR1B. Interacts with HECTD1. Ref.7 Ref.8 Ref.9

Subcellular location

Isoform 1: Membrane; Multi-pass membrane protein Potential.

Isoform 2: Membrane; Multi-pass membrane protein Potential.

Isoform 3: Secreted Potential.

Tissue specificity

Highly expressed in pancreas, testis and fetal liver. Moderately expressed in heart, prostate and small intestine. Expressed at very low levels in brain, thymus, ovary, colon, fetal lung and fetal kidney. Expressed in muscle. Isoform 3 is expressed in pituitary gland. Ref.2 Ref.3

Sequence similarities

Contains 12 Ig-like C2-type (immunoglobulin-like) domains.

Caution

It is uncertain whether Met-1 or Met-12 is the initiator.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q8N6C5-1)

Also known as: InhBP-L; long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N6C5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     24-33: RMSLGMTSIV → L
Isoform 3 (identifier: Q8N6C5-3)

Also known as: InhBP-S; short;

The sequence of this isoform differs from the canonical sequence as follows:
     224-242: LYPKPTLTAHPGPIMAPGE → GCGYGCWHLAIVVPGIMAG
     243-1336: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 13361308Immunoglobulin superfamily member 1
PRO_0000318512

Regions

Topological domain29 – 518490Extracellular Potential
Transmembrane519 – 53921Helical; Potential
Topological domain540 – 55920Cytoplasmic Potential
Transmembrane560 – 58021Helical; Potential
Topological domain581 – 1336756Extracellular Potential
Domain38 – 12285Ig-like C2-type 1
Domain137 – 22286Ig-like C2-type 2
Domain226 – 31287Ig-like C2-type 3
Domain321 – 40888Ig-like C2-type 4
Domain419 – 50082Ig-like C2-type 5
Domain589 – 67789Ig-like C2-type 6
Domain686 – 76075Ig-like C2-type 7
Domain777 – 86993Ig-like C2-type 8
Domain873 – 95886Ig-like C2-type 9
Domain965 – 106096Ig-like C2-type 10
Domain1065 – 115086Ig-like C2-type 11
Domain1161 – 124282Ig-like C2-type 12

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation6071N-linked (GlcNAc...) Potential
Glycosylation7471N-linked (GlcNAc...) Potential
Glycosylation7981N-linked (GlcNAc...) Potential
Glycosylation8461N-linked (GlcNAc...) Potential
Glycosylation9391N-linked (GlcNAc...) Potential
Glycosylation9861N-linked (GlcNAc...) Potential
Glycosylation10271N-linked (GlcNAc...) Potential
Glycosylation10821N-linked (GlcNAc...) Potential
Glycosylation11471N-linked (GlcNAc...) Potential
Glycosylation12231N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 106 By similarity
Disulfide bond248 ↔ 296 By similarity
Disulfide bond343 ↔ 392 By similarity
Disulfide bond441 ↔ 484 By similarity
Disulfide bond703 ↔ 750 By similarity
Disulfide bond799 ↔ 849 By similarity
Disulfide bond895 ↔ 942 By similarity
Disulfide bond1087 ↔ 1134 By similarity
Disulfide bond1183 ↔ 1226 By similarity

Natural variations

Alternative sequence24 – 3310RMSLGMTSIV → L in isoform 2.
VSP_031195
Alternative sequence224 – 24219LYPKP…MAPGE → GCGYGCWHLAIVVPGIMAG in isoform 3.
VSP_031196
Alternative sequence243 – 13361094Missing in isoform 3.
VSP_031197
Natural variant3811N → H.
Corresponds to variant rs6637826 [ dbSNP | Ensembl ].
VAR_054960

Experimental info

Sequence conflict4621K → R in CAA71535. Ref.1
Sequence conflict4941I → M in CAA71535. Ref.1
Sequence conflict7571R → L in CAA71535. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (InhBP-L) (long) [UniParc].

Last modified April 14, 2009. Version 3.
Checksum: 7D0D2C36FD1CE8B8

FASTA1,336148,936
        10         20         30         40         50         60 
MTLDRPGEGA TMLKTFTVLL FCIRMSLGMT SIVMDPQPEL WIESNYPQAP WENITLWCRS 

        70         80         90        100        110        120 
PSRISSKFLL LKDKTQMTWI RPSHKTFQVS FLIGALTESN AGLYRCCYWK ETGWSKPSKV 

       130        140        150        160        170        180 
LELEAPGQLP KPIFWIQAET PALPGCNVNI LCHGWLQDLV FMLFKEGYAE PVDYQVPTGT 

       190        200        210        220        230        240 
MAIFSIDNLT PEDEGVYICR THIQMLPTLW SEPSNPLKLV VAGLYPKPTL TAHPGPIMAP 

       250        260        270        280        290        300 
GESLNLRCQG PIYGMTFALM RVEDLEKSFY HKKTIKNEAN FFFQSLKIQD TGHYLCFYYD 

       310        320        330        340        350        360 
ASYRGSLLSD VLKIWVTDTF PKTWLLARPS AVVQMGQNVS LRCRGPVDGV GLALYKKGED 

       370        380        390        400        410        420 
KPLQFLDATS IDDNTSFFLN NVTYSDTGIY SCHYLLTWKT SIRMPSHNTV ELMVVDKPPK 

       430        440        450        460        470        480 
PSLSAWPSTV FKLGKAITLQ CRVSHPVLEF SLEWEERETF QKFSVNGDFI ISNVDGKGTG 

       490        500        510        520        530        540 
TYSCSYRVET HPNIWSHRSE PLKLMGPAGY LTWNYVLNEA IRLSLIMQLV ALLLVVLWIR 

       550        560        570        580        590        600 
WKCRRLRIRE AWLLGTAQGV TMLFIVTALL CCGLCNGVLI EETEIVMPTP KPELWAETNF 

       610        620        630        640        650        660 
PLAPWKNLTL WCRSPSGSTK EFVLLKDGTG WIATRPASEQ VRAAFPLGAL TQSHTGSYHC 

       670        680        690        700        710        720 
HSWEEMAVSE PSEALELVGT DILPKPVISA SPTIRGQELQ LRCKGWLAGM GFALYKEGEQ 

       730        740        750        760        770        780 
EPVQQLGAVG REAFFTIQRM EDKDEGNYSC RTHTEKRPFK WSEPSEPLEL VIKEMYPKPF 

       790        800        810        820        830        840 
FKTWASPVVT PGARVTFNCS TPHQHMSFIL YKDGSEIASS DRSWASPGAS AAHFLIISVG 

       850        860        870        880        890        900 
IGDGGNYSCR YYDFSIWSEP SDPVELVVTE FYPKPTLLAQ PGPVVFPGKS VILRCQGTFQ 

       910        920        930        940        950        960 
GMRFALLQEG AHVPLQFRSV SGNSADFLLH TVGAEDSGNY SCIYYETTMS NRGSYLSMPL 

       970        980        990       1000       1010       1020 
MIWVTDTFPK PWLFAEPSSV VPMGQNVTLW CRGPVHGVGY ILHKEGEATS MQLWGSTSND 

      1030       1040       1050       1060       1070       1080 
GAFPITNISG TSMGRYSCCY HPDWTSSIKI QPSNTLELLV TGLLPKPSLL AQPGPMVAPG 

      1090       1100       1110       1120       1130       1140 
ENMTLQCQGE LPDSTFVLLK EGAQEPLEQQ RPSGYRADFW MPAVRGEDSG IYSCVYYLDS 

      1150       1160       1170       1180       1190       1200 
TPFAASNHSD SLEIWVTDKP PKPSLSAWPS TMFKLGKDIT LQCRGPLPGV EFVLEHDGEE 

      1210       1220       1230       1240       1250       1260 
APQQFSEDGD FVINNVEGKG IGNYSCSYRL QAYPDIWSEP SDPLELVGAA GPVAQECTVG 

      1270       1280       1290       1300       1310       1320 
NIVRSSLIVV VVVALGVVLA IEWKKWPRLR TRGSETDGRD QTIALEECNQ EGEPGTPANS 

      1330 
PSSTSQRISV ELPVPI 

« Hide

Isoform 2 [UniParc].

Checksum: 736C689FEC94D2E1
Show »

FASTA1,327147,973
Isoform 3 (InhBP-S) (short) [UniParc].

Checksum: 1F8A2B1484A754EB
Show »

FASTA24227,206

References

« Hide 'large scale' references
[1]"Identification and genomic organization of a gene coding for a new member of the cell adhesion molecule family mapping to Xq25."
Frattini A., Faranda S., Redolfi E., Allavena P., Vezzoni P.
Gene 214:1-6(1998) [PubMed: 9729118] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning and expression of an immunoglobulin superfamily gene (IGSF1) in Xq25."
Mazzarella R., Pengue G., Jones J., Jones C., Schlessinger D.
Genomics 48:157-162(1998) [PubMed: 9521868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[3]"Expression profile of active genes in the human pituitary gland."
Tanaka S., Tatsumi K., Okubo K., Itoh K., Kawamoto S., Matsubara K., Amino N.
J. Mol. Endocrinol. 28:33-44(2002) [PubMed: 11854097] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
Tissue: Pituitary.
[4]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed: 9205841] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[5]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1153-1336.
Tissue: Testis.
[7]"Modulation of activin signal transduction by inhibin B and inhibin-binding protein (INhBP)."
Chapman S.C., Woodruff T.K.
Mol. Endocrinol. 15:668-679(2001) [PubMed: 11266516] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACVR1B; ACVR2A; ACVR2B; ACVRL1 AND BMPR1B.
[8]"Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs."
Nakayama M., Kikuno R., Ohara O.
Genome Res. 12:1773-1784(2002) [PubMed: 12421765] [Abstract]
Cited for: INTERACTION WITH HECTD1.
[9]"Properties of inhibin binding to betaglycan, InhBP/p120 and the activin type II receptors."
Chapman S.C., Bernard D.J., Jelen J., Woodruff T.K.
Mol. Cell. Endocrinol. 196:79-93(2002) [PubMed: 12385827] [Abstract]
Cited for: NEGATIVE INTERACTION WITH INHA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10523 mRNA. Translation: CAA71535.1.
AF034198 mRNA. Translation: AAC52057.1.
AB058894 mRNA. Translation: BAB40235.1.
AB002362 mRNA. Translation: BAA20819.2.
AL590806 Genomic DNA. No translation available.
AL137369 mRNA. Translation: CAB70713.1.
IPIIPI00043215.
IPI00166985.
IPI00515081.
RefSeqNP_001164433.1. NM_001170962.1.
NP_001164434.1. NM_001170963.1.
NP_001546.2. NM_001555.4.
NP_991402.1. NM_205833.3.
UniGeneHs.22111.

3D structure databases

HSSPHSSP built from PDB template 1OVZ based on UniProtKB P24071.
ProteinModelPortalQ8N6C5.
SMRQ8N6C5. Positions 36-1319.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8N6C5. 2 interactions.
STRINGQ8N6C5.

PTM databases

PhosphoSiteQ8N6C5.

Polymorphism databases

DMDM226694182.

Proteomic databases

PRIDEQ8N6C5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361420; ENSP00000355010; ENSG00000147255.
GeneID3547.
KEGGhsa:3547.
UCSCuc004ewd.1. human.
uc004ewf.1. human.
uc004ewg.1. human.

Organism-specific databases

CTD3547.
GeneCardsGC0XM130407.
H-InvDBHIX0017051.
HGNCHGNC:5948. IGSF1.
MIM300137. gene.
neXtProtNX_Q8N6C5.
PharmGKBPA29761.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07894.
GeneTreeENSGT00570000078816.
HOGENOMHBG507240.
OMACSYRLQA.

Gene expression databases

ArrayExpressQ8N6C5.
BgeeQ8N6C5.
CleanExHS_IGSF1.
GenevestigatorQ8N6C5.

Family and domain databases

InterProIPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 12 hits.
PfamPF00047. ig. 1 hit.
[Graphical view]
SMARTSM00409. IG. 6 hits.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio13848.
SOURCESearch...

Entry information

Entry nameIGSF1_HUMAN
AccessionPrimary (citable) accession number: Q8N6C5
Secondary accession number(s): B5MEG2, O15070, Q9NTC8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 14, 2009
Last modified: January 25, 2012
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families